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1ESN

STRUCTURAL BASIS FOR THE FEEDBACK REGULATION OF ESCHERICHIA COLI PANTOTHENATE KINASE BY COENZYME A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004594molecular_functionpantothenate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0015937biological_processcoenzyme A biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0042803molecular_functionprotein homodimerization activity
A0050165molecular_functionpantetheine kinase activity
B0000166molecular_functionnucleotide binding
B0004594molecular_functionpantothenate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0015937biological_processcoenzyme A biosynthetic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0042803molecular_functionprotein homodimerization activity
B0050165molecular_functionpantetheine kinase activity
C0000166molecular_functionnucleotide binding
C0004594molecular_functionpantothenate kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0015937biological_processcoenzyme A biosynthetic process
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0016740molecular_functiontransferase activity
C0042803molecular_functionprotein homodimerization activity
C0050165molecular_functionpantetheine kinase activity
D0000166molecular_functionnucleotide binding
D0004594molecular_functionpantothenate kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0015937biological_processcoenzyme A biosynthetic process
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
D0016740molecular_functiontransferase activity
D0042803molecular_functionprotein homodimerization activity
D0050165molecular_functionpantetheine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
ASER102
AGLU199
AANP401

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BSER102
BGLU199
BANP402

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 503
ChainResidue
CSER102
CGLU199
CANP403

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG D 504
ChainResidue
DSER102
DGLU199
DANP404

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ANP A 401
ChainResidue
AASN43
AASP45
ALEU46
ATYR55
AVAL97
AALA98
AVAL99
AGLY100
ALYS101
ASER102
ATHR103
AGLU199
AARG243
ALYS303
AHIS307
AMG501
AHOH5136

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ANP B 402
ChainResidue
BASN43
BASP45
BTYR55
BVAL97
BALA98
BVAL99
BGLY100
BLYS101
BSER102
BTHR103
BGLU199
BARG243
BLYS303
BHIS307
BMG502
BHOH5077
BHOH5104
BHOH5209

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ANP C 403
ChainResidue
CASN43
CASP45
CVAL97
CALA98
CVAL99
CGLY100
CLYS101
CSER102
CTHR103
CGLU199
CARG243
CLYS303
CHIS307
CMG503
CHOH5064
CHOH5221
CHOH5263

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ANP D 404
ChainResidue
DASN43
DASP45
DTYR55
DVAL97
DALA98
DVAL99
DGLY100
DLYS101
DSER102
DTHR103
DARG243
DLYS303
DHIS307
DMG504
DHOH5110
DHOH5306

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY95
BGLY95
CGLY95
DGLY95

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PDB entries from 2024-04-24

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